EC Number   |
Metals/Ions |
Reference |
|---|
    1.7.2.4 | Ca2+ |
1.2 atoms per subunit |
394533 |
| 1.7.2.4 | Ca2+ |
single Ca2+ ion binds to the Ca2+-binding loop coordinated by residues Y251, E255, M263, D269, and S316 and a water molecule, Ca2+ plays a role in secondary structure stabilization during maturation of nitrous oxide reductase, required for structural stability of the binuclear CuA site |
741924 |
| 1.7.2.4 | Ca2+ |
two calcium sites located at the intermonomeric surface |
394516 |
| 1.7.2.4 | copper |
3.2 mol of copper per mol of enzyme, in the as-isolated form. Presence of 0.1 mM enhances enzymic activity by 2fold |
724958 |
| 1.7.2.4 | copper |
dependent on. The enzyme nitrous oxide reductase contains two copper sites: a binuclear site known as CuA that functions as an electron transfer site, and an unusual tetranuclear copper sulfide cluster active site, where N2O binds and is reduced. Two forms of this tetranuclear site have been structurally characterized. One, known as CuZ*, has a mu4 sulfide ligand bridging all four coppers and a solvent derived ligand on an open edge (the CuI-CuIV edge) where N2O is proposed to bind. The other form of the cluster, known as CuZ, has an additional mu2 sulfur ligand bridging the CuI-CuIV edge. Raman spectroscopic analysis and computationa modelling of Cu site structure and mechanism, binding and interaction, overview. Protonation state of the mu2 sulfur ligand on the CuI-CuIV edge in 1-hole and 2-hole CuZ |
742272 |
| 1.7.2.4 | copper |
form A and B contain 9.0 and 8.2 Cu atoms per dimer, respectively |
659085 |
| 1.7.2.4 | copper |
multicopper enzyme, 2 copper centers per subunit, CuA and CuZ |
659880 |
| 1.7.2.4 | copper |
N2OR contains two copper centers, CuA, a binuclear mixed-valence center and CuZ, a tetranuclear sulfide-bridged copper cluster |
660478 |
| 1.7.2.4 | copper |
the fully reduced all-Cu(I) state of CuZ is the catalytically relevant redox state of N2OR |
658979 |
| 1.7.2.4 | Cu |
- |
394526, 394527, 394528, 394540, 394541, 394542 |
